1B4W

BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS-IMPLICATIONS FOR ITS ASSOCIATION AND ANTICOAGULANT ACTIVITIES BY X-RAY CRYSTALLOGRAPHY

1B4W の概要

• エントリーDOI: 10.2210/pdb1b4w/pdb
• 分子名称: PROTEIN (PHOSPHOLIPASE A2), octyl beta-D-glucopyranoside (3 entities in total)
• 機能のキーワード: basic phospholipase a2, agkistrodon halys pallas, dimer, anticoagulant activity, hydrolase
• 由来する生物種: Gloydius halys (halys viper)
• 細胞内の位置: Secreted: O42187
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 56277.41

構造登録者

Zhao, K.H.,Lin, Z.J. (登録日: 1998-12-30, 公開日: 2000-01-12, 最終更新日: 2024-10-16)

主引用文献

Zhao, K.,Zhou, Y.,Lin, Z.
Structure of basic phospholipase A2 from Agkistrodon halys Pallas: implications for its association, hemolytic and anticoagulant activities.
Toxicon, 38:901-916, 2000

PubMed Abstract: The basic phospholipase A2 (PLA2) from the venom of Agkistrodon halys Pallas is a potent hemolytic toxin and anticoagulant. Crystal structure of the enzyme complexed with detergent n-octyl beta-D-glucopyranoside (beta-OG) in monoclinic crystal form has been determined to 2.6 A resolution. Beta-OG molecules were found in the hydrophobic channels of the enzyme. SDS-PAGE and dynamic light scattering measurements showed that the enzyme had a strong tendency to dimerise in aqueous solution. In the crystal structure the enzyme molecules associate into a tetramer with pseudo 222 symmetry, and the interfacial recognition site linked dimers constituting the tetramer have intensive interface interactions, and may be stable in solution. The structure reveals a unique positively charged face at the C-terminal region and a characteristic non-cationic 'anticoagulant' region (53-77). The face is supposed to be the hemolytic site, and based on sequence and structure comparison residues Trp70 and Glu53 instead of the basic residues in 'anticoagulant' region might play an important role in the anticoagulant activity.

PubMed: 10728829
DOI: 10.1016/S0041-0101(99)00193-2

実験手法

X-RAY DIFFRACTION (2.6 Å)